Phospholipase C-γ1 potentiates integrin-dependent cell spreading and migration through Pyk2/paxillin activation

2007 ◽  
Vol 19 (8) ◽  
pp. 1784-1796 ◽  
Author(s):  
J CHOI ◽  
Y YANG ◽  
S LEE ◽  
I KIM ◽  
S HA ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Cell Spreading ◽  
Dependent Cell ◽  
And Migration

scholarly journals RLIP76 regulates Arf6-dependent cell spreading and migration by linking ARNO with activated R-Ras at recycling endosomes

2015 ◽  
Vol 467 (4) ◽  
pp. 785-791 ◽  
Author(s):  
Jeremy G.T. Wurtzel ◽  
Seunghyung Lee ◽  
Sharad S. Singhal ◽  
Sanjay Awasthi ◽  
Mark H. Ginsberg ◽  
...  
Keyword(s):  
Cell Spreading ◽  
Recycling Endosomes ◽  
Dependent Cell ◽  
And Migration

scholarly journals Mac-1 Promotes FcγRIIA-Dependent Cell Spreading and Migration on Immune Complexes†

Biochemistry ◽  
2006 ◽  
Vol 45 (29) ◽  
pp. 8721-8731 ◽  
Author(s):  
Ying Xiong ◽  
Chunzhang Cao ◽  
Alexandra Makarova ◽  
Brad Hyman ◽  
Li Zhang
Keyword(s):  
Immune Complexes ◽  
Cell Spreading ◽  
Dependent Cell ◽  
And Migration

scholarly journals The Unique N-Terminus of R-Ras Is Required for Rac Activation and Precise Regulation of Cell Migration

2005 ◽  
Vol 16 (5) ◽  
pp. 2458-2469 ◽  
Author(s):  
Stephen P. Holly ◽  
Mark K. Larson ◽  
Leslie V. Parise
Keyword(s):  
Cell Migration ◽  
Cell Movement ◽  
Myeloid Cell ◽  
Cell Spreading ◽  
Full Length ◽  
Structural Basis ◽  
N Terminus ◽  
Cellular Behaviors ◽  
Dependent Cell ◽  
And Migration

The Ras family GTPase, R-Ras, elicits important integrin-dependent cellular behaviors such as adhesion, spreading and migration. While oncogenic Ras GTPases and R-Ras share extensive sequence homology, R-Ras induces a distinct set of cellular behaviors. To explore the structural basis for these differences, we asked whether the unique N-terminal 26 amino acid extension of R-Ras was responsible for R-Ras–specific signaling events. Using a 32D mouse myeloid cell line, we show that full-length R-Ras activates Rac and induces Rac-dependent cell spreading. In contrast, truncated R-Ras lacking its first 26 amino acids fails to activate Rac, resulting in reduced cell spreading. Truncated R-Ras also stimulates more β3 integrin-dependent cell migration than full-length R-Ras, suggesting that the N-terminus may negatively regulate cell movement. However, neither the subcellular localization of R-Ras nor its effects on cell adhesion are affected by the presence or absence of the N-terminus. These results indicate that the N-terminus of R-Ras positively regulates specific R-Ras functions such as Rac activation and cell spreading but negatively regulates R-Ras–mediated cell migration.

scholarly journals Clustering of Syndecan-4 and Integrin β1 by Laminin α3 Chain–derived Peptide Promotes Keratinocyte Migration

2009 ◽  
Vol 20 (13) ◽  
pp. 3012-3024 ◽  
Author(s):  
Eri Araki ◽  
Yutaka Momota ◽  
Takeshi Togo ◽  
Miki Tanioka ◽  
Kentaro Hozumi ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Chronic Wound ◽  
Cell Spreading ◽  
Integrin Β1 ◽  
Keratinocyte Migration ◽  
Dependent Cell ◽  
And Migration ◽  
Binding Sequence

Syndecans function as receptors for extracellular matrix (ECM) with integrins in cell spreading. However, the molecular mechanism of their specific involvement in cell migration or in wound healing has not been elucidated yet. Here, we report that a synthetic peptide, PEP75, which contains the syndecan-binding sequence of the laminin α3LG4 module, induces keratinocyte migration in in vitro and in vivo. Soluble PEP75 induced the clustering of syndecan-4 and conformation-modified integrin β1 colocalized with syndecan-4 in soluble PEP75-induced clusters. Treatment of cells in solution with PEP75 resulted in the exposure of the P4G11 antibody epitope of integrin β1 in immunostaining as well as in flow cytometry and augmented integrin β1–dependent cell adhesion to ECM. Pulldown assays demonstrated that PEP75 bound to syndecan-4, but not to integrin β1. A siRNA study revealed a role for syndecan-4 in PEP75-induced up-regulation of P4G11 antibody binding and migration of HaCaT cells. We conclude that binding of soluble PEP75 to syndecan-4 induces the coupling of integrin β1, which is associated with integrin β1-conformational changes and activation, and leads to keratinocyte migration. To activate integrin function through syndecans could be a novel therapeutic approach for chronic wound.

scholarly journals The syndecan-1 ectodomain regulates αvβ3 integrin activity in human mammary carcinoma cells

2004 ◽  
Vol 167 (1) ◽  
pp. 171-181 ◽  
Author(s):  
DeannaLee M. Beauvais ◽  
Brandon J. Burbach ◽  
Alan C. Rapraeger
Keyword(s):  
Mammary Carcinoma ◽  
Ectopic Expression ◽  
Cell Spreading ◽  
Αvβ3 Integrin ◽  
Growth Factor Signaling ◽  
Small Interfering Rnas ◽  
Human Mammary Carcinoma ◽  
Dependent Cell ◽  
Mammary Carcinoma Cells ◽  
And Migration

The αvβ3 integrin participates in cell morphogenesis, growth factor signaling, and cell survival. Activation of the integrin is central to these processes and is influenced by specific ECM components, which engage both integrins and syndecans. This paper demonstrates that the αvβ3 integrin and syndecan-1 (S1) are functionally coupled. The integrin is dependent on the syndecan to become activated and to mediate signals required for MDA-MB-231 and MDA-MB-435 human mammary carcinoma cell spreading on vitronectin or S1-specific antibody. Coupling of the syndecan to αvβ3 requires the S1 ectodomain (ED), as ectopic expression of glycosylphosphatidylinositol-linked S1ED enhances αvβ3 recognition of vitronectin; and treatments that target this domain, including competition with recombinant S1ED protein or anti-S1ED antibodies, mutation of the S1ED, or down-regulation of S1 expression by small-interfering RNAs, disrupt αvβ3-dependent cell spreading and migration. Thus, S1 is likely to be a critical regulator of many cellular behaviors that depend on activated αvβ3 integrins.

Nanopatterned Adhesive, Stretchable Hydrogel to Control Ligand Spacing and Regulate Cell Spreading and Migration

ACS Nano ◽  
2017 ◽  
Vol 11 (8) ◽  
pp. 8282-8291 ◽  
Author(s):  
Jie Deng ◽  
Changsheng Zhao ◽  
Joachim P. Spatz ◽  
Qiang Wei
Keyword(s):  
Cell Spreading ◽  
And Migration

Distinct signals via Rho GTPases and Src drive shape changes by thrombin and sphingosine-1-phosphate in endothelial cells

2002 ◽  
Vol 115 (12) ◽  
pp. 2475-2484 ◽  
Author(s):  
Valérie Vouret-Craviari ◽  
Christine Bourcier ◽  
Etienne Boulter ◽  
Ellen Van Obberghen-Schilling
Keyword(s):  
Endothelial Cells ◽  
Rho Gtpases ◽  
Actin Polymerization ◽  
Morphological Changes ◽  
Umbilical Vein ◽  
Cell Spreading ◽  
Actin Binding ◽  
Sphingosine 1 Phosphate ◽  
And Migration ◽  
Umbilical Vein Endothelial Cells

Soluble mediators such as thrombin and sphingosine-1-phosphate regulate morphological changes in endothelial cells that affect vascular permeability and new blood vessel formation. Although these ligands activate a similar set of heterotrimeric G proteins, thrombin causes cell contraction and rounding whereas sphingosine-1-phosphate induces cell spreading and migration. A functional requirement for Rho family GTPases in the cytoskeletal responses to both ligands has been established, yet the dynamics of their regulation and additional signaling mechanisms that lead to such opposite effects remain poorly understood. Using a pull-down assay to monitor the activity of Rho GTPases in human umbilical vein endothelial cells, we find significant temporal and quantitative differences in RhoA and Rac1 activation. High levels of active RhoA rapidly accumulate in cells in response to thrombin whereas Rac1 is inhibited. In contrast, sphingosine-1-phosphate addition leads to comparatively weak and delayed activation of RhoA and it activates Rac1. In addition, we show here that sphingosine-1-phosphate treatment activates a Src family kinase and triggers recruitment of the F-actin-binding protein cortactin to sites of actin polymerization at the rim of membrane ruffles. Both Src and Rac pathways are essential for lamellipodia targeting of cortactin. Further, Src plays a determinant role in sphingosine-1-phosphate-induced cell spreading and migration. Taken together these data demonstrate that the thrombin-induced contractile and immobile phenotype in endothelial cells reflects both robust RhoA activation and Rac inhibition, whereas Src- and Rac-dependent events couple sphingosine-1-phosphate receptors to the actin polymerizing machinery that drives the extension of lamellipodia and cell migration.

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